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UniProtKB - P06897 (H2A1_XENLA)

Entry version 154 (29 Sep 2021)
Sequence version 2 (23 Jan 2007)
Previous versions | rss
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Protein

Histone H2A type 1

Gene
N/A
Organism
Xenopus laevis (African clawed frog)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionDNA-binding

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Histone H2A type 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiXenopus laevis (African clawed frog)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri8355 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Amphibia › Batrachia › Anura › Pipoidea › Pipidae › Xenopodinae › Xenopus › Xenopus

Organism-specific databases

Xenopus laevis and tropicalis biology and genomics resource

More...Xenbasei		XB-GENE-6493983, h2ax.lS

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000552942 – 130Histone H2A type 1Add BLAST129

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineBy similarity1
Modified residuei2PhosphoserineBy similarity1
Modified residuei6N6-(2-hydroxyisobutyryl)lysineBy similarity1
Modified residuei6N6-acetyllysineBy similarity1
Modified residuei10N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei10N6-lactoyllysine; alternateBy similarity1
Modified residuei10N6-succinyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki16Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei37N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei75N6-(2-hydroxyisobutyryl)lysineBy similarity1
Modified residuei76N6-(2-hydroxyisobutyryl)lysineBy similarity1
Modified residuei96N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei96N6-glutaryllysine; alternateBy similarity1
Modified residuei96N6-succinyllysineBy similarity1
Modified residuei105N5-methylglutamineBy similarity1
Modified residuei119N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity1
Modified residuei119N6-glutaryllysine; alternateBy similarity1
Cross-linki120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Monoubiquitination of Lys-120 (H2AK119Ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties, leading to the recruitment of repair proteins to sites of DNA damage. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events (By similarity).By similarity
Phosphorylation on Ser-2 is enhanced during mitosis. Phosphorylation on Ser-2 directly represses transcription (By similarity).By similarity
Glutamine methylation at Gln-105 (H2AQ104me) by FBL is specifically dedicated to polymerase I. It is present at 35S ribosomal DNA locus and impairs binding of the FACT complex (By similarity).By similarity

Keywords - PTMi

Acetylation, Hydroxylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		592527, 5 interactors

Database of interacting proteins

More...DIPi		DIP-39144N

Protein interaction database and analysis system

More...IntActi		P06897, 16 interactors

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1130
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Small Angle Scattering Biological Data Bank

More...SASBDBi		P06897

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P06897

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P06897

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 22DisorderedSequence analysisAdd BLAST22

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the histone H2A family.Curated

Phylogenomic databases

Database of Orthologous Groups

More...OrthoDBi		1504122at2759

Family and domain databases

Conserved Domains Database

More...CDDi		cd00074, H2A, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.20.10, 1 hit

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...IDEALi		IID50139

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR009072, Histone-fold
IPR002119, Histone_H2A
IPR007125, Histone_H2A/H2B/H3
IPR032454, Histone_H2A_C
IPR032458, Histone_H2A_CS

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00125, Histone, 1 hit
PF16211, Histone_H2A_C, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00620, HISTONEH2A

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00414, H2A, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF47113, SSF47113, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00046, HISTONE_H2A, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P06897-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV 
        60         70         80         90        100
YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVRN DEELNKLLGG 
       110        120        130
VTIAQGGVLP NIQSVLLPKK TESAKSAKSK
Length:130
Mass (Da):13,966
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i09946ABF27FA52A9
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X03018 Genomic DNA Translation: CAA26817.1
M21287 Genomic DNA Translation: AAA49769.1
BC106331 mRNA Translation: AAI06332.1

Protein sequence database of the Protein Information Resource

More...PIRi		H24510, HSXLA1

NCBI Reference Sequences

More...RefSeqi		NP_001089684.1, NM_001096215.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		734746

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		xla:734746

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03018 Genomic DNA Translation: CAA26817.1
M21287 Genomic DNA Translation: AAA49769.1
BC106331 mRNA Translation: AAI06332.1
PIRiH24510, HSXLA1
RefSeqiNP_001089684.1, NM_001096215.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AOIX-ray2.80C/G5-120[»]
1KX3X-ray2.00C/G2-130[»]
1KX4X-ray2.60C/G2-130[»]
1KX5X-ray1.94C/G2-130[»]
1M18X-ray2.45C/G2-130[»]
1M19X-ray2.30C/G2-130[»]
1M1AX-ray2.65C/G2-130[»]
1P34X-ray2.70C/G2-130[»]
1P3AX-ray3.00C/G2-130[»]
1P3BX-ray3.00C/G2-130[»]
1P3FX-ray2.90C/G2-130[»]
1P3GX-ray2.70C/G2-130[»]
1P3IX-ray2.30C/G2-130[»]
1P3KX-ray2.90C/G2-130[»]
1P3LX-ray2.40C/G2-130[»]
1P3MX-ray2.90C/G2-130[»]
1P3OX-ray2.75C/G2-130[»]
1P3PX-ray2.70C/G2-130[»]
1S32X-ray2.05C/G2-120[»]
1ZBBX-ray9.00C/G/c/g2-130[»]
1ZLAX-ray2.90C/G2-130[»]
2FJ7X-ray3.20C/G2-130[»]
2NZDX-ray2.65C/G2-120[»]
3B6FX-ray3.45C/G2-130[»]
3B6GX-ray3.45C/G2-130[»]
3C1BX-ray2.20C/G2-130[»]
3C1CX-ray3.15C/G2-130[»]
3KUYX-ray2.90C/G2-120[»]
3KWQX-ray3.50C/G15-121[»]
3LJAX-ray2.75C/G2-130[»]
3MNNX-ray2.50C/G2-120[»]
3O62X-ray3.22C/G2-130[»]
3REHX-ray2.50C/G2-130[»]
3REIX-ray2.65C/G2-130[»]
3REJX-ray2.55C/G2-130[»]
3REKX-ray2.60C/G2-130[»]
3RELX-ray2.70C/G2-130[»]
3TU4X-ray3.00C/G2-130[»]
3UT9X-ray2.20C/G2-130[»]
3UTAX-ray2.07C/G2-130[»]
3UTBX-ray2.20C/G2-130[»]
4J8UX-ray2.38C/G2-130[»]
4J8VX-ray2.58C/G2-130[»]
4J8WX-ray2.41C/G2-130[»]
4J8XX-ray2.87C/G2-130[»]
4LD9X-ray3.31C/G1-130[»]
4R8PX-ray3.28C/G2-130[»]
4WU8X-ray2.45C/G2-130[»]
4WU9X-ray2.60C/G2-130[»]
4XUJX-ray3.18C/G2-130[»]
4XZQX-ray2.40C/G15-121[»]
4YS3X-ray3.00C/G15-121[»]
4Z66X-ray2.50C/G15-121[»]
4ZUXX-ray3.82C/G/M/Q1-130[»]
5CP6X-ray2.60C/G2-130[»]
5DNMX-ray2.81C/G2-130[»]
5DNNX-ray2.80C/G2-130[»]
5E5AX-ray2.81C/G1-130[»]
5F99X-ray2.63C/G2-130[»]
5G2EX-ray6.70C/G/K/O/S/W14-119[»]
5HQ2X-ray4.50G2-130[»]
5MLUX-ray2.80C/G15-119[»]
5NL0X-ray5.40C/G/M2-130[»]
5O9Gelectron microscopy4.80C/G1-130[»]
5OMXX-ray2.32C/G2-130[»]
5ONGX-ray2.80C/G2-130[»]
5ONWX-ray2.80C/G2-130[»]
5OXVX-ray6.72C/G/M/Q1-130[»]
5OY7X-ray5.77C/G/K/O/S/W/a/e1-130[»]
5X0Xelectron microscopy3.97C/G1-130[»]
5X0Yelectron microscopy4.69C/G2-130[»]
5XF6X-ray2.63C/G2-130[»]
5Z3Lelectron microscopy4.31C/G2-130[»]
5Z3Oelectron microscopy3.62C/G2-130[»]
6FQ5electron microscopy3.80C/G10-119[»]
6FQ6electron microscopy4.00C/G10-119[»]
6FQ8electron microscopy4.80C/G10-119[»]
6FTXelectron microscopy4.50C/G1-130[»]
6G0Lelectron microscopy4.50C/G1-130[»]
6I84electron microscopy4.40Q/V1-130[»]
6IROelectron microscopy3.40C/G2-130[»]
6IY2electron microscopy3.47C/G10-122[»]
6IY3electron microscopy3.67C/G10-122[»]
6KIUelectron microscopy3.20C/G2-130[»]
6KIVelectron microscopy4.00C/G2-130[»]
6KIWelectron microscopy4.00C/G2-130[»]
6KIXelectron microscopy4.10C/G2-130[»]
6KIZelectron microscopy4.50C/G2-130[»]
6KW3electron microscopy7.13O/S1-130[»]
6KW4electron microscopy7.55O/S1-130[»]
6KW5electron microscopy10.13O/T1-130[»]
6LTJelectron microscopy3.70C/G1-130[»]
6N1ZX-ray2.70B/E1-130[»]
6NE3electron microscopy3.90C/G1-130[»]
6NJ9electron microscopy2.96C/G2-130[»]
6NN6electron microscopy3.90C/G2-130[»]
6NOGelectron microscopy3.90C/G2-130[»]
6NQAelectron microscopy3.54C/G2-130[»]
6NZOelectron microscopy3.80C/G18-130[»]
6O96electron microscopy3.50C/G1-130[»]
6OM3X-ray3.30C/G/O/S1-130[»]
6PA7electron microscopy2.94C/G2-130[»]
6PWVelectron microscopy6.20I/M2-130[»]
6PWWelectron microscopy4.40I/M2-130[»]
6PWXelectron microscopy4.20I/M2-130[»]
6PX1electron microscopy3.30C/G18-130[»]
6PX3electron microscopy4.10C/G18-130[»]
6R1Telectron microscopy3.70C/G11-121[»]
6R1Uelectron microscopy4.36C/G2-130[»]
6R25electron microscopy4.61C/G2-130[»]
6RYRelectron microscopy3.10C/G1-130[»]
6RYUelectron microscopy4.00C/G1-130[»]
6S01electron microscopy3.20C/G2-130[»]
6T9Lelectron microscopy3.60C/G2-130[»]
6TDAelectron microscopy15.00C/G2-130[»]
6TEMelectron microscopy3.90C/G2-130[»]
6UXWelectron microscopy8.96T/X2-130[»]
6VENelectron microscopy3.37C/G2-130[»]
6VYPX-ray4.99C/G/c/g2-130[»]
6W4LX-ray1.31A14-105[»]
6W5Melectron microscopy4.60I/M2-130[»]
6W5Nelectron microscopy6.00I/M2-130[»]
6WKRelectron microscopy3.50K/R1-130[»]
6WZ5electron microscopy2.20C/G2-130[»]
6WZ9electron microscopy2.80C/G2-130[»]
6X0Nelectron microscopy10.00C/G/c/g2-130[»]
6Z6Pelectron microscopy4.43G15-119[»]
6ZHXelectron microscopy2.50C/G1-130[»]
6ZHYelectron microscopy3.00C1-130[»]
7CROelectron microscopy3.75C/G2-130[»]
7CRPelectron microscopy3.20C/G2-130[»]
7CRQelectron microscopy3.15C/G2-130[»]
7CRRelectron microscopy3.48C/G2-130[»]
7K6Pelectron microscopy3.20C/G13-119[»]
7K6Qelectron microscopy3.10C/G13-119[»]
SASBDBiP06897
SMRiP06897
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi592527, 5 interactors
DIPiDIP-39144N
IntActiP06897, 16 interactors

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		734746

Genome annotation databases

GeneIDi734746
KEGGixla:734746

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		734746
XenbaseiXB-GENE-6493983, h2ax.lS

Phylogenomic databases

OrthoDBi1504122at2759

Miscellaneous databases

EvolutionaryTraceiP06897

Family and domain databases

CDDicd00074, H2A, 1 hit
Gene3Di1.10.20.10, 1 hit
IDEALiIID50139
InterProiView protein in InterPro
IPR009072, Histone-fold
IPR002119, Histone_H2A
IPR007125, Histone_H2A/H2B/H3
IPR032454, Histone_H2A_C
IPR032458, Histone_H2A_CS
PfamiView protein in Pfam
PF00125, Histone, 1 hit
PF16211, Histone_H2A_C, 1 hit
PRINTSiPR00620, HISTONEH2A
SMARTiView protein in SMART
SM00414, H2A, 1 hit
SUPFAMiSSF47113, SSF47113, 1 hit
PROSITEiView protein in PROSITE
PS00046, HISTONE_H2A, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiH2A1_XENLA
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P06897
Secondary accession number(s): Q3B8I8
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 154 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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